Acetylcholine binding by a synthetic receptor: implications for biological recognition.
The neurotransmitter acetylcholine (ACh) is bound with 50-micromolar affinity by a completely synthetic receptor (host) comprising primarily aromatic rings. The host provided an overall hydrophobic binding site, but one that could recognize the positive charge of the quaternary ammonium group of ACh through a stabilizing interaction with the electron-rich pi systems of the aromatic rings (cation-pi interaction). Similar interactions may be involved in biological recognition of ACh and other choline derivatives.
Dougherty
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Arnold and Mabel Beckman Laboratories of Chemical Synthesis, California Institute of Technology, Pasadena 91125.
Stauffer
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D000109:Acetylcholine / Q000378:metabolism*; D000345:Affinity Labels; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002412:Cations; D004330:Drosophila; D004563:Electrochemistry; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010767:Phosphorylcholine / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics; D014101:Torpedo
D000345:Affinity Labels; D002412:Cations; D007140:Immunoglobulin Fab Fragments; D000644:Quaternary Ammonium Compounds; D011950:Receptors, Cholinergic; D010767:Phosphorylcholine; D000109:Acetylcholine